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Stephanie Federico

Tenured professor

University of Trieste
Country flagItaly

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About

Stephanie Federico is a tenured professor at the University of Trieste, Italy. Her research primarily focuses on the structural investigation and molecular modeling of adenosine receptors, protein kinase inhibitors, and neurodegenerative disease mechanisms. Recent publications highlight her work on novel inhibitors and their implications in cancer and amyotrophic lateral sclerosis. She is dedicated to advancing the understanding of GPCRs and their therapeutic potential.

Positions (1)

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University of Trieste

University of Trieste

Multiple PhD positions are available in Italy for the 2025/2026 academic year across leading universities including the University of Trieste, University of Verona, University of Bari, University of Salento, University of Perugia, University of Siena, University of Catania, University of Messina, and University of Cagliari. Research areas span Chemistry, Materials Science, Nanosciences, Biomolecular Sciences, Chemical and Molecular Science, and Pharmaceutical Sciences. These programs are highly interdisciplinary, covering advanced chemical processes, innovative materials, nanotechnology, and applications in industrial, biomedical, and environmental sectors. Applicants must typically hold a relevant master's degree or an equivalent foreign qualification. The selection process generally involves an assessment of academic qualifications and an oral interview, which may be conducted remotely. English language proficiency is tested during the interview. Some programs, such as at the University of Bari, offer multiple funded positions, including scholarships and externally co-financed places. The University of Trieste's Chemistry PhD program, for example, requires applications by June 6, 2025, with interviews in July. Other universities have similar competitive selection processes and deadlines, with early international notices often closing in January. Funding varies by institution and program, with some offering full or partial scholarships, and others requiring payment of registration fees (with possible exemptions for certain countries). Detailed funding information and eligibility criteria are provided in each university's call for applications. Prospective students are encouraged to review the official program links and calls for applications for specific requirements, deadlines, and application procedures. Supervisors and coordinators for these programs include tenured professors such as Stephanie Federico, Emanuele Coccia, Jacopo Dosso, Giovanna Fronzoni, Tatiana Da Ros, Michele Melchionna (University of Trieste), and Prof. Pietro Favia (University of Bari). These faculty members are involved in the selection and supervision of PhD candidates. To apply, candidates should visit the official PhD program websites, register online, and submit all required documents, including CV, degree certificates, and any specific forms. It is essential to read the full call for applications for each program to ensure compliance with all requirements and deadlines. The programs offer a vibrant research environment in Italy, with opportunities to work on cutting-edge topics in chemistry, materials science, and related fields.

1 year ago

Articles (14)

Year:

2025

Protein kinase CK1δ (CK1δ) is a serine-threonine/kinase that modulates different physiological processes, including the cell cycle, DNA repair, and apoptosis. CK1δ overexpression, and the consequent hyperphosphorylation of specific proteins, can lead to sleep disorders, cancer, and neurodegenerative diseases. CK1δ inhibitors showed anticancer properties as well as neuroprotective effects in cellular and animal models of Parkinson’s and Alzheimer’s diseases and amyotrophic lateral sclerosis. To obtain new ATP-competitive CK1δ inhibitors, three sets of benzimidazole-2-amino derivatives were synthesized (1–32), bearing different substituents on the fused benzo ring (R) and diverse pyrazole-containing acyl moieties on the 2-amino group. The best-performing derivatives were those featuring the (1H-pyrazol-3-yl)-acetyl moiety on the benzimidazol-2-amino scaffold (13–32), which showed CK1δ inhibitor activity in the low micromolar range. Among the R substituents, 5-cyano was the most advantageous, leading to a compound endowed with nanomolar potency (23, IC50 = 98.6 nM). Molecular docking and dynamics studies were performed to point out the inhibitor–kinase interactions.

Year:

2024

Year:

2023

Year:

2023

Year:

2023

The A 3 adenosine receptor is an interesting target whose role in cancer is controversial. In this work, a structural investigation at the 2‐position of the [1,2,4]triazolo[1,5‐ c ]pyrimidine nucleus was performed, finding new potent and selective A 3 adenosine receptor antagonists such as the ethyl 2‐(4‐methoxyphenyl)‐5‐(methylamino)‐[1,2,4]triazolo[1,5‐ c ]pyrimidine‐8‐carboxylate ( 20 , DZ123) that showed a K i value of 0.47 nM and an exceptional selectivity profile over the other adenosine receptor subtypes. Computational studies were performed to rationalize the affinity and the selectivity profile of the tested compounds at the A 3 adenosine receptor and the A 1 and A 2A adenosine receptors. Compound 20 was tested on both A 3 adenosine receptor positive cell lines (CHO‐A 3 AR transfected, THP1 and HCT16) and on A 3 negative cancer cell lines, showing no effect in the latter and a pro‐proliferative effect at a low concentration in the former. These interesting results pave the way to further investigation on both the mechanism involved and potential therapeutic applications.

Year:

2023

Year:

2023

Year:

2022

Year:

2022

Year:

2022

Year:

2021

Year:

2021

Year:

2020

Year:

2020

Collaborators (7)

Tatiana Da Ros

Tenured professor

University of Trieste

ITALY
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Mattia Sturlese

University of Padova

ITALY
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Rosaria Volpini

University of Camerino

ITALY
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Giampiero Spalluto

-

ITALY
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Vittoria Colotta

University of Florence

ITALY
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Fabrizio Vincenzi

University of Ferrara

ITALY
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Stefano Moro

Professor of Medicinal Chemistry

University of Padova

ITALY
View details
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